The interaction of alkaline and acid phosphatase with oxovanadium (IV) and vanadium (IV) ions will be investigated using kinetic and electron paramagnetic resonance techniques. The potent competitive inhibition of these phosphate-hydrolyzing enzymes indicates their active site binding and thus potential as probes of enzyme mechanism and structure. Amino acid analogs with boron in the place of the carboxyl carbon have been prepared in impure form. More specific dipeptide analogs will be synthesized as potential tetrahedral intermediate adduct analogs for proteolytic enzymes. Kinetic studies will be carried out to elucidate the nature of the enzyme inhibitor interactions. Human placental ceramide trihexosidase will be encapsulated and its properties studied. Sensitivity to pH changes and acrylamide monomer have led to inactive preparations to date. Affinity chromatography will be used to purify the active ceramide trihexosidase from nonspecific alpha-galactosidases.